SECA2_GEOKA
ID SECA2_GEOKA Reviewed; 797 AA.
AC Q5KV31;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein translocase subunit SecA 2 {ECO:0000255|HAMAP-Rule:MF_01382};
DE EC=7.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01382};
GN Name=secA2 {ECO:0000255|HAMAP-Rule:MF_01382}; OrderedLocusNames=GK3170;
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426;
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC the SecYEG preprotein conducting channel. Has a central role in
CC coupling the hydrolysis of ATP to the transfer of proteins into and
CC across the cell membrane, serving as an ATP-driven molecular motor
CC driving the stepwise translocation of polypeptide chains across the
CC membrane. {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + cellular proteinSide 1 = ADP + phosphate +
CC cellular proteinSide 2.; EC=7.4.2.8; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01382};
CC -!- SUBUNIT: Monomer and homodimer. Part of the essential Sec protein
CC translocation apparatus which comprises SecA, SecYEG and auxiliary
CC proteins SecDF. Other proteins may also be involved.
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01382};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01382};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01382}. Cytoplasm
CC {ECO:0000255|HAMAP-Rule:MF_01382}. Note=Distribution is 50-50.
CC {ECO:0000255|HAMAP-Rule:MF_01382}.
CC -!- SIMILARITY: Belongs to the SecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01382}.
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DR EMBL; BA000043; BAD77455.1; -; Genomic_DNA.
DR RefSeq; WP_011232640.1; NC_006510.1.
DR AlphaFoldDB; Q5KV31; -.
DR SMR; Q5KV31; -.
DR STRING; 235909.GK3170; -.
DR EnsemblBacteria; BAD77455; BAD77455; GK3170.
DR KEGG; gka:GK3170; -.
DR PATRIC; fig|235909.7.peg.3382; -.
DR eggNOG; COG0653; Bacteria.
DR HOGENOM; CLU_005314_3_2_9; -.
DR OMA; IGQIHEF; -.
DR Proteomes; UP000001172; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008564; F:protein-exporting ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0017038; P:protein import; IEA:InterPro.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR CDD; cd18803; SF2_C_secA; 1.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_01382; SecA; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000185; SecA.
DR InterPro; IPR030908; SecA2_Bac_anthr.
DR InterPro; IPR020937; SecA_CS.
DR InterPro; IPR011115; SecA_DEAD.
DR InterPro; IPR014018; SecA_motor_DEAD.
DR InterPro; IPR011130; SecA_preprotein_X-link_dom.
DR InterPro; IPR044722; SecA_SF2_C.
DR InterPro; IPR011116; SecA_Wing/Scaffold.
DR InterPro; IPR036266; SecA_Wing/Scaffold_sf.
DR InterPro; IPR036670; SecA_X-link_sf.
DR PANTHER; PTHR30612; PTHR30612; 1.
DR Pfam; PF07517; SecA_DEAD; 1.
DR Pfam; PF01043; SecA_PP_bind; 1.
DR Pfam; PF07516; SecA_SW; 1.
DR PRINTS; PR00906; SECA.
DR SMART; SM00957; SecA_DEAD; 1.
DR SMART; SM00958; SecA_PP_bind; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF81767; SSF81767; 1.
DR SUPFAM; SSF81886; SSF81886; 1.
DR TIGRFAMs; TIGR00963; secA; 1.
DR TIGRFAMs; TIGR04397; SecA2_Bac_anthr; 1.
DR PROSITE; PS01312; SECA; 1.
DR PROSITE; PS51196; SECA_MOTOR_DEAD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding;
KW Protein transport; Reference proteome; Translocase; Translocation;
KW Transport.
FT CHAIN 1..797
FT /note="Protein translocase subunit SecA 2"
FT /id="PRO_0000318356"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 103..107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01382"
SQ SEQUENCE 797 AA; 91340 MW; 90EAD0C9452EEF94 CRC64;
MFAKVKQLFD ESAREVQRLA KLAAQINEWE PTISSLSDEQ LRQKTVVFKE RLERGETLDD
IKIEAFAVVR EAARRVLGLR HYDVQLMGGL AMHEGNIAEM QTGEGKTLAA TLPSYLHALL
GKGVHIITAN EYLARRDCEQ MGRVFRFLGL TVGLNVSQMT ASEKKEAYAA DITYGTGTEF
GFDYLRDNMV YRLEDKVQRP LYYAIIDEID SILIDEARTP LIIANKSGIG AELFPIMARI
VRTFEEGKEY ERSLETKQIF LTEEGAQKIE RAFGIDNLYD WEHHVLLHHA MQSLRAWFIM
RRDVDYIVKN GKVMIVDPFT GRVMEGRSFS DGLHQAIEAK EGVEITEEND IQATITIQNY
FRMYEKLAGM TGSATPSKEE FWQTYRLRVI TIPTNQPSRR TDWDDLVYQT YEAKVRKIID
EVKKMNAIGR PVLIGTTSVA QSEQLSAAFS KAGIPHHLLN AKTEEEEARI IATAGQKGQV
MIATNMAGRG TDILLGEGVK ELGGLHIIGT ERHESHRIDM QLRGRAGRQG DPGSSQFIIS
LDDDLFRLYD QDELKKWKSK VETDETGRIV SPDPIKFVQK VQTTIENAHY SARLHLLKLD
TVIDQQSKVI YHMRDRVLAL KQAEVLSELL RHIHRHITQT IDRYCPENVF FEEWNIEGLH
NELRRAFFRF AYPIDDLRHK QKEEIAQLVW DEYKSLEAAL ADLPCDEEQT MRLKHLMVET
IDAHWIRHLN QLNLLKEGIH LRSYGQEDPY RAFEMDAYRE FVALQQAIDA GICTTAMNYL
KSQFVIDDEA AAAANKP
